5C4K

APH(2")-IVa in complex with GET (G418) at room temperature

Summary for 5C4K

• Entry DOI: 10.2210/pdb5c4k/pdb
• Descriptor: APH(2'')-Id, GENETICIN (2 entities in total)
• Functional Keywords: aminoglycoside phosphotransferase, antibiotic resistance, transferase
• Biological source: Enterococcus casseliflavus
• Total number of polymer chains: 2
• Total formula weight: 75688.26

Authors

Kaplan, E.,Guichou, J.F.,Berrou, K.,Chaloin, L.,Leban, N.,Lallemand, P.,Barman, T.,Serpersu, E.H.,Lionne, C. (deposition date: 2015-06-18, release date: 2016-02-03, Last modification date: 2024-01-10)

Primary citation

Kaplan, E.,Guichou, J.F.,Chaloin, L.,Kunzelmann, S.,Leban, N.,Serpersu, E.H.,Lionne, C.
Aminoglycoside binding and catalysis specificity of aminoglycoside 2-phosphotransferase IVa: A thermodynamic, structural and kinetic study.
Biochim.Biophys.Acta, 1860:802-813, 2016

PubMed Abstract: Aminoglycoside O-phosphotransferases make up a large class of bacterial enzymes that is widely distributed among pathogens and confer a high resistance to several clinically used aminoglycoside antibiotics. Aminoglycoside 2″-phosphotransferase IVa, APH(2″)-IVa, is an important member of this class, but there is little information on the thermodynamics of aminoglycoside binding and on the nature of its rate-limiting step.

PubMed: 26802312
DOI: 10.1016/j.bbagen.2016.01.016

Experimental method

X-RAY DIFFRACTION (3.05 Å)